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. Author manuscript; available in PMC: 2012 Apr 12.
Published in final edited form as: Nature. 2011 Aug 28;477(7365):495–498. doi: 10.1038/nature10370

Figure 2. PIP2 binding site.

Figure 2

a, A detailed view of the PIP2 binding site is shown in the same orientation as outlined in figure 1c. Helices (shown as ribbon) from different subunits are colored orange and cyan interior. Residues hydrogen bonded (dashed lines) to PIP2 are colored green, and residues stabilizing the PIP2 binding site in the CTD while lacking direct contact are colored blue. All side chains are shown as sticks. PIP2 is shown as sticks and colored according to atom type: carbon, yellow; phosphorous, orange; and oxygen, red. b, An amino acid sequence alignment of selected eukaryotic Kirs showing residues predicted from literature (blue outline) and not predicted (purple outline) to interact with PIP29,28. Residues with direct bonding interactions to PIP2 and with a structural role are highlighted with green and blue shade, respectively. The two residues serving as the inner helix gate are also highlighted with grey shade.